Structural basis of p63α SAM domain mutants involved in AEC syndrome - Wikidata - awgldk - TriplyDB

Structural basis of p63α SAM domain mutants involved in AEC syndrome

Structural basis of p63α SAM domain mutants involved in AEC syndrome

http://www.wikidata.org/entity/Q27668032

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Structure and Kinetic Stability of the p63 Tetramerization Domain Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factor Special AT-rich binding protein-2 (SATB2) differentially affects disease-causing p63 mutant proteins.Repression of Wnt/β-catenin response elements by p63 (TP63)Quality control in oocytes by p63 is based on a spring-loaded activation mechanism on the molecular and cellular level.Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome.Intrinsic aggregation propensity of the p63 and p73 TI domains correlates with p53R175H interaction and suggests further significance of aggregation events in the p53 family.Novel variant in the TP63 gene associated to ankyloblepharon-ectodermal dysplasia-cleft lip/palate (AEC) syndrome.

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

http://www.wikidata.org/entity/Q27668032

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2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

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type

label

Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

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prefLabel

Structural basis of p63α SAM domain mutants involved in AEC syndrome

@ast

Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Structural basis of p63α SAM domain mutants involved in AEC syndrome

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Aruna Sathyamurthy

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Christopher M Johnson

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Mark Bycroft

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Mark D Allen

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Stefan M V Freund

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P2860

p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities

Cloning and functional analysis of human p51, which structurally and functionally resembles p53

Complex transcriptional effects of p63 isoforms: identification of novel activation and repression domains

Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha

RNA recognition via the SAM domain of Smaug

NMR Studies of a Heterotypic Sam−Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor † , ‡

Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy

Version 1.2 of the Crystallography and NMR system

Solving structures of protein complexes by molecular replacement with Phaser

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